UniProtKB - P06897 (H2A1_XENLA)
Protein
Histone H2A type 1
Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Functioni
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- protein heterodimerization activity Source: InterPro
Keywordsi
Molecular function | DNA-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H2A type 1 |
Organismi | Xenopus laevis (African clawed frog) |
Taxonomic identifieri | 8355 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus |
Organism-specific databases
Xenbasei | XB-GENE-6493983, h2ax.lS |
Subcellular locationi
Nucleus
Other locations
Nucleus
- nucleus Source: UniProtKB-SubCell
Other locations
- nucleosome Source: UniProtKB-KW
Keywords - Cellular componenti
Chromosome, Nucleosome core, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000055294 | 2 – 130 | Histone H2A type 1Add BLAST | 129 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineBy similarity | 1 | |
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 6 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 6 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 10 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 10 | N6-succinyllysineBy similarity | 1 | |
Cross-linki | 14 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Cross-linki | 16 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
Modified residuei | 37 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 75 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 76 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 96 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 96 | N6-glutaryllysine; alternateBy similarity | 1 | |
Modified residuei | 96 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 105 | N5-methylglutamineBy similarity | 1 | |
Modified residuei | 119 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 119 | N6-glutaryllysine; alternateBy similarity | 1 | |
Cross-linki | 120 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity |
Post-translational modificationi
Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity).By similarity
Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription (By similarity).By similarity
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (By similarity).By similarity
Keywords - PTMi
Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationInteractioni
Subunit structurei
The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.
GO - Molecular functioni
- protein heterodimerization activity Source: InterPro
Protein-protein interaction databases
BioGRIDi | 592527, 4 interactors |
DIPi | DIP-39144N |
IntActi | P06897, 16 interactors |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SASBDBi | P06897 |
SMRi | P06897 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P06897 |
Family & Domainsi
Sequence similaritiesi
Belongs to the histone H2A family.Curated
Phylogenomic databases
OrthoDBi | 1504122at2759 |
Family and domain databases
CDDi | cd00074, H2A, 1 hit |
Gene3Di | 1.10.20.10, 1 hit |
IDEALi | IID50139 |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR002119, Histone_H2A IPR007125, Histone_H2A/H2B/H3 IPR032454, Histone_H2A_C IPR032458, Histone_H2A_CS |
Pfami | View protein in Pfam PF00125, Histone, 1 hit PF16211, Histone_H2A_C, 1 hit |
PRINTSi | PR00620, HISTONEH2A |
SMARTi | View protein in SMART SM00414, H2A, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00046, HISTONE_H2A, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P06897-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV
60 70 80 90 100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG
110 120 130
VTIAQGGVLP NIQSVLLPKK TESAKSAKSK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X03018 Genomic DNA Translation: CAA26817.1 M21287 Genomic DNA Translation: AAA49769.1 BC106331 mRNA Translation: AAI06332.1 |
PIRi | H24510, HSXLA1 |
RefSeqi | NP_001089684.1, NM_001096215.1 |
Genome annotation databases
GeneIDi | 734746 |
KEGGi | xla:734746 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X03018 Genomic DNA Translation: CAA26817.1 M21287 Genomic DNA Translation: AAA49769.1 BC106331 mRNA Translation: AAI06332.1 |
PIRi | H24510, HSXLA1 |
RefSeqi | NP_001089684.1, NM_001096215.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AOI | X-ray | 2.80 | C/G | 5-120 | [»] | |
1KX3 | X-ray | 2.00 | C/G | 2-130 | [»] | |
1KX4 | X-ray | 2.60 | C/G | 2-130 | [»] | |
1KX5 | X-ray | 1.94 | C/G | 2-130 | [»] | |
1M18 | X-ray | 2.45 | C/G | 2-130 | [»] | |
1M19 | X-ray | 2.30 | C/G | 2-130 | [»] | |
1M1A | X-ray | 2.65 | C/G | 2-130 | [»] | |
1P34 | X-ray | 2.70 | C/G | 2-130 | [»] | |
1P3A | X-ray | 3.00 | C/G | 2-130 | [»] | |
1P3B | X-ray | 3.00 | C/G | 2-130 | [»] | |
1P3F | X-ray | 2.90 | C/G | 2-130 | [»] | |
1P3G | X-ray | 2.70 | C/G | 2-130 | [»] | |
1P3I | X-ray | 2.30 | C/G | 2-130 | [»] | |
1P3K | X-ray | 2.90 | C/G | 2-130 | [»] | |
1P3L | X-ray | 2.40 | C/G | 2-130 | [»] | |
1P3M | X-ray | 2.90 | C/G | 2-130 | [»] | |
1P3O | X-ray | 2.75 | C/G | 2-130 | [»] | |
1P3P | X-ray | 2.70 | C/G | 2-130 | [»] | |
1S32 | X-ray | 2.05 | C/G | 2-120 | [»] | |
1ZBB | X-ray | 9.00 | C/G/c/g | 2-130 | [»] | |
1ZLA | X-ray | 2.90 | C/G | 2-130 | [»] | |
2FJ7 | X-ray | 3.20 | C/G | 2-130 | [»] | |
2NZD | X-ray | 2.65 | C/G | 2-120 | [»] | |
3B6F | X-ray | 3.45 | C/G | 2-130 | [»] | |
3B6G | X-ray | 3.45 | C/G | 2-130 | [»] | |
3C1B | X-ray | 2.20 | C/G | 2-130 | [»] | |
3C1C | X-ray | 3.15 | C/G | 2-130 | [»] | |
3KUY | X-ray | 2.90 | C/G | 2-120 | [»] | |
3KWQ | X-ray | 3.50 | C/G | 15-121 | [»] | |
3LJA | X-ray | 2.75 | C/G | 2-130 | [»] | |
3MNN | X-ray | 2.50 | C/G | 2-120 | [»] | |
3O62 | X-ray | 3.22 | C/G | 2-130 | [»] | |
3REH | X-ray | 2.50 | C/G | 2-130 | [»] | |
3REI | X-ray | 2.65 | C/G | 2-130 | [»] | |
3REJ | X-ray | 2.55 | C/G | 2-130 | [»] | |
3REK | X-ray | 2.60 | C/G | 2-130 | [»] | |
3REL | X-ray | 2.70 | C/G | 2-130 | [»] | |
3TU4 | X-ray | 3.00 | C/G | 2-130 | [»] | |
3UT9 | X-ray | 2.20 | C/G | 2-130 | [»] | |
3UTA | X-ray | 2.07 | C/G | 2-130 | [»] | |
3UTB | X-ray | 2.20 | C/G | 2-130 | [»] | |
4J8U | X-ray | 2.38 | C/G | 2-130 | [»] | |
4J8V | X-ray | 2.58 | C/G | 2-130 | [»] | |
4J8W | X-ray | 2.41 | C/G | 2-130 | [»] | |
4J8X | X-ray | 2.87 | C/G | 2-130 | [»] | |
4LD9 | X-ray | 3.31 | C/G | 1-130 | [»] | |
4R8P | X-ray | 3.28 | C/G | 2-130 | [»] | |
4WU8 | X-ray | 2.45 | C/G | 2-130 | [»] | |
4WU9 | X-ray | 2.60 | C/G | 2-130 | [»] | |
4XUJ | X-ray | 3.18 | C/G | 2-130 | [»] | |
4XZQ | X-ray | 2.40 | C/G | 15-121 | [»] | |
4YS3 | X-ray | 3.00 | C/G | 15-121 | [»] | |
4Z66 | X-ray | 2.50 | C/G | 15-121 | [»] | |
4ZUX | X-ray | 3.82 | C/G/M/Q | 1-130 | [»] | |
5CP6 | X-ray | 2.60 | C/G | 2-130 | [»] | |
5DNM | X-ray | 2.81 | C/G | 2-130 | [»] | |
5DNN | X-ray | 2.80 | C/G | 2-130 | [»] | |
5E5A | X-ray | 2.81 | C/G | 1-130 | [»] | |
5F99 | X-ray | 2.63 | C/G | 2-130 | [»] | |
5G2E | X-ray | 6.70 | C/G/K/O/S/W | 14-119 | [»] | |
5HQ2 | X-ray | 4.50 | G | 2-130 | [»] | |
5MLU | X-ray | 2.80 | C/G | 15-119 | [»] | |
5NL0 | X-ray | 5.40 | C/G/M | 2-130 | [»] | |
5O9G | electron microscopy | 4.80 | C/G | 1-130 | [»] | |
5OMX | X-ray | 2.32 | C/G | 2-130 | [»] | |
5ONG | X-ray | 2.80 | C/G | 2-130 | [»] | |
5ONW | X-ray | 2.80 | C/G | 2-130 | [»] | |
5OXV | X-ray | 6.72 | C/G/M/Q | 1-130 | [»] | |
5OY7 | X-ray | 5.77 | C/G/K/O/S/W/a/e | 1-130 | [»] | |
5X0X | electron microscopy | 3.97 | C/G | 1-130 | [»] | |
5X0Y | electron microscopy | 4.69 | C/G | 2-130 | [»] | |
5XF6 | X-ray | 2.63 | C/G | 2-130 | [»] | |
5Z3L | electron microscopy | 4.31 | C/G | 2-130 | [»] | |
5Z3O | electron microscopy | 3.62 | C/G | 2-130 | [»] | |
6FQ5 | electron microscopy | 3.80 | C/G | 10-119 | [»] | |
6FQ6 | electron microscopy | 4.00 | C/G | 10-119 | [»] | |
6FQ8 | electron microscopy | 4.80 | C/G | 10-119 | [»] | |
6FTX | electron microscopy | 4.50 | C/G | 1-130 | [»] | |
6G0L | electron microscopy | 4.50 | C/G | 1-130 | [»] | |
6I84 | electron microscopy | 4.40 | Q/V | 1-130 | [»] | |
6IRO | electron microscopy | 3.40 | C/G | 2-130 | [»] | |
6IY2 | electron microscopy | 3.47 | C/G | 10-122 | [»] | |
6IY3 | electron microscopy | 3.67 | C/G | 10-122 | [»] | |
6KIU | electron microscopy | 3.20 | C/G | 2-130 | [»] | |
6KIV | electron microscopy | 4.00 | C/G | 2-130 | [»] | |
6KIW | electron microscopy | 4.00 | C/G | 2-130 | [»] | |
6KIX | electron microscopy | 4.10 | C/G | 2-130 | [»] | |
6KIZ | electron microscopy | 4.50 | C/G | 2-130 | [»] | |
6KW3 | electron microscopy | 7.13 | O/S | 1-130 | [»] | |
6KW4 | electron microscopy | 7.55 | O/S | 1-130 | [»] | |
6KW5 | electron microscopy | 10.13 | O/T | 1-130 | [»] | |
6LTJ | electron microscopy | 3.70 | C/G | 1-130 | [»] | |
6N1Z | X-ray | 2.70 | B/E | 1-130 | [»] | |
6NE3 | electron microscopy | 3.90 | C/G | 1-130 | [»] | |
6NJ9 | electron microscopy | 2.96 | C/G | 2-130 | [»] | |
6NN6 | electron microscopy | 3.90 | C/G | 2-130 | [»] | |
6NOG | electron microscopy | 3.90 | C/G | 2-130 | [»] | |
6NQA | electron microscopy | 3.54 | C/G | 2-130 | [»] | |
6NZO | electron microscopy | 3.80 | C/G | 18-130 | [»] | |
6O96 | electron microscopy | 3.50 | C/G | 1-130 | [»] | |
6OM3 | X-ray | 3.30 | C/G/O/S | 1-130 | [»] | |
6PA7 | electron microscopy | 2.94 | C/G | 2-130 | [»] | |
6PWV | electron microscopy | 6.20 | I/M | 2-130 | [»] | |
6PWW | electron microscopy | 4.40 | I/M | 2-130 | [»] | |
6PWX | electron microscopy | 4.20 | I/M | 2-130 | [»] | |
6PX1 | electron microscopy | 3.30 | C/G | 18-130 | [»] | |
6PX3 | electron microscopy | 4.10 | C/G | 18-130 | [»] | |
6R1T | electron microscopy | 3.70 | C/G | 11-121 | [»] | |
6R1U | electron microscopy | 4.36 | C/G | 2-130 | [»] | |
6R25 | electron microscopy | 4.61 | C/G | 2-130 | [»] | |
6RYR | electron microscopy | 3.10 | C/G | 1-130 | [»] | |
6RYU | electron microscopy | 4.00 | C/G | 1-130 | [»] | |
6S01 | electron microscopy | 3.20 | C/G | 2-130 | [»] | |
6T9L | electron microscopy | 3.60 | C/G | 2-130 | [»] | |
6TDA | electron microscopy | 15.00 | C/G | 2-130 | [»] | |
6TEM | electron microscopy | 3.90 | C/G | 2-130 | [»] | |
6UXW | electron microscopy | 8.96 | T/X | 2-130 | [»] | |
6VEN | electron microscopy | 3.37 | C/G | 2-130 | [»] | |
6VYP | X-ray | 4.99 | C/G/c/g | 2-130 | [»] | |
6W4L | X-ray | 1.31 | A | 14-105 | [»] | |
6WZ5 | electron microscopy | 2.20 | C/G | 2-130 | [»] | |
6WZ9 | electron microscopy | 2.80 | C/G | 2-130 | [»] | |
6X0N | electron microscopy | 10.00 | C/G/c/g | 2-130 | [»] | |
SASBDBi | P06897 | |||||
SMRi | P06897 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 592527, 4 interactors |
DIPi | DIP-39144N |
IntActi | P06897, 16 interactors |
Genome annotation databases
GeneIDi | 734746 |
KEGGi | xla:734746 |
Organism-specific databases
CTDi | 734746 |
Xenbasei | XB-GENE-6493983, h2ax.lS |
Phylogenomic databases
OrthoDBi | 1504122at2759 |
Miscellaneous databases
EvolutionaryTracei | P06897 |
Family and domain databases
CDDi | cd00074, H2A, 1 hit |
Gene3Di | 1.10.20.10, 1 hit |
IDEALi | IID50139 |
InterProi | View protein in InterPro IPR009072, Histone-fold IPR002119, Histone_H2A IPR007125, Histone_H2A/H2B/H3 IPR032454, Histone_H2A_C IPR032458, Histone_H2A_CS |
Pfami | View protein in Pfam PF00125, Histone, 1 hit PF16211, Histone_H2A_C, 1 hit |
PRINTSi | PR00620, HISTONEH2A |
SMARTi | View protein in SMART SM00414, H2A, 1 hit |
SUPFAMi | SSF47113, SSF47113, 1 hit |
PROSITEi | View protein in PROSITE PS00046, HISTONE_H2A, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | H2A1_XENLA | |
Accessioni | P06897Primary (citable) accession number: P06897 Secondary accession number(s): Q3B8I8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1988 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 10, 2021 | |
This is version 151 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families